Structure of PDB 8i07 Chain F Binding Site BS01

Receptor Information
>8i07 Chain F (length=594) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GMAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILAR
HVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILC
ITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHL
MRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEM
LIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHE
LMAGMVGLQTAHRYGNATLLASDMVFGIGNRFAQRHTGSVEKYTEGRKIV
HIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWV
ADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIA
AAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDF
QFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQMAFDMDYCVQLAFENI
NSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPV
VVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE
Ligand information
Ligand IDTPP
InChIInChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain8i07 Chain D Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8i07 Engineering of two thiamine diphosphate-dependent enzymes for the regioselective condensation of C1-formaldehyde into C4-erythrulose
Resolution1.99 Å
Binding residue
(original residue number in PDB)		V51 T75
Binding residue
(residue number reindexed from 1)		V52 T76
Annotation score1
Enzymatic activity
Enzyme Commision number 4.1.1.47: tartronate-semialdehyde synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0009028 tartronate-semialdehyde synthase activity
GO:0016829 lyase activity
GO:0030976 thiamine pyrophosphate binding
GO:0042802 identical protein binding
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0009097 isoleucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0009436 glyoxylate catabolic process
GO:0019752 carboxylic acid metabolic process
GO:0046296 glycolate catabolic process
Cellular Component
GO:0005948 acetolactate synthase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8i07, PDBe:8i07, PDBj:8i07
PDBsum8i07
PubMed37890751
UniProtP0AEP7|GCL_ECOLI Glyoxylate carboligase (Gene Name=gcl)

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